MGRB_ECO27
ID MGRB_ECO27 Reviewed; 47 AA.
AC B7USK2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=PhoP/PhoQ regulator MgrB {ECO:0000255|HAMAP-Rule:MF_01596};
GN Name=mgrB {ECO:0000255|HAMAP-Rule:MF_01596}; OrderedLocusNames=E2348C_1950;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- FUNCTION: PhoP-regulated transcription is redox-sensitive, being
CC activated when the periplasm becomes more reducing. MgrB acts between
CC DsbA/DsbB and PhoP/PhoQ in this pathway. Represses PhoP/PhoQ signaling,
CC possibly by binding to the periplasmic domain of PhoQ, altering its
CC activity and that of downstream effector PhoP. {ECO:0000255|HAMAP-
CC Rule:MF_01596}.
CC -!- SUBUNIT: May form homooligomers. Probably interacts with the
CC periplasmic domain of PhoQ. {ECO:0000255|HAMAP-Rule:MF_01596}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01596}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01596}.
CC -!- SIMILARITY: Belongs to the MgrB family. {ECO:0000255|HAMAP-
CC Rule:MF_01596}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM180568; CAS09498.1; -; Genomic_DNA.
DR RefSeq; WP_000714544.1; NC_011601.1.
DR AlphaFoldDB; B7USK2; -.
DR EnsemblBacteria; CAS09498; CAS09498; E2348C_1950.
DR KEGG; ecg:E2348C_1950; -.
DR HOGENOM; CLU_208030_1_0_6; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070298; P:negative regulation of phosphorelay signal transduction system; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01596; MgrB; 1.
DR InterPro; IPR020907; MgrB.
DR Pfam; PF13998; MgrB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..47
FT /note="PhoP/PhoQ regulator MgrB"
FT /id="PRO_1000185764"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01596"
SQ SEQUENCE 47 AA; 5524 MW; 337A0378D23CDDC0 CRC64;
MKKFRWVALV VVVLACLLLW AQVFNMMCDQ DVQFFSGICA INQFIPW